Lectin-induced alterations of the interaction of insulin and insulin-like growth factor 1 receptors with their ligands

In order to study whether the carbohydrate moieties of the human placental IGF-I receptor (IGF1R), IGF-II receptor (IGF2R) and insulin receptors (IRs) play a role in ligand binding, solubilised cell membrane preparations were incubated with 125I-labelled IGF-I, IGF-II and insulin in the presence of...

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Bibliographic Details
Main Authors: ROMANA MASNIKOSA, ANNA J. NIKOLIC, OLGICA NEDIC
Format: Article
Language:English
Published: Serbian Chemical Society 2008-08-01
Series:Journal of the Serbian Chemical Society
Subjects:
Online Access:http://www.shd.org.yu/JSCS/Vol73/No8-9/JSCS-3762.pdf
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Summary:In order to study whether the carbohydrate moieties of the human placental IGF-I receptor (IGF1R), IGF-II receptor (IGF2R) and insulin receptors (IRs) play a role in ligand binding, solubilised cell membrane preparations were incubated with 125I-labelled IGF-I, IGF-II and insulin in the presence of lectins with different sugar specificities. Three incubation procedures were tested: ligand-first, co-incubation and lectin-first incubation. Wheat germ agglutinin (WGA), concanavalin A (Con A) and phytohaemagglutinin (PHA) altered the binding of IGF-I and insulin to their high-affinity receptors in a lectin specific and dose-dependent manner, whereas these lectins did not affect the interaction of IGF-II with its receptor(s). Moreover, the same lectins either inhibited or enhanced IGF-I and insulin binding, depending on the incubation scheme. These results also suggest that IR-A and IR-B from human placenta might be differently glycosylated.
ISSN:0352-5139